GLCD_ECOLI
ID GLCD_ECOLI Reviewed; 499 AA.
AC P0AEP9; P52075; Q2M9L6;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Glycolate oxidase subunit GlcD {ECO:0000305|PubMed:8606183};
DE EC=1.1.99.14 {ECO:0000269|PubMed:4557653, ECO:0000305|PubMed:8606183};
DE AltName: Full=Glycolate dehydrogenase subunit GlcD;
GN Name=glcD {ECO:0000303|PubMed:8606183}; Synonyms=gox, yghM;
GN OrderedLocusNames=b2979, JW2946;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE,
RP INDUCTION, AND SUBUNIT.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8606183; DOI=10.1128/jb.178.7.2051-2059.1996;
RA Pellicer M.T., Badia J., Aguilar J.T., Baldoma L.;
RT "glc locus of Escherichia coli: characterization of genes encoding the
RT subunits of glycolate oxidase and the glc regulator protein.";
RL J. Bacteriol. 178:2051-2059(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RC STRAIN=K12;
RX PubMed=4557653; DOI=10.1016/0005-2728(72)90111-9;
RA Lord J.M.;
RT "Glycolate oxidoreductase in Escherichia coli.";
RL Biochim. Biophys. Acta 267:227-237(1972).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 11775;
RX PubMed=2689218; DOI=10.1016/0014-5793(89)81673-4;
RA Sallal A.K., Nimer N.A.;
RT "The intracellular localization of glycolate oxidoreductase in Escherichia
RT coli.";
RL FEBS Lett. 258:277-280(1989).
RN [6]
RP INDUCTION.
RC STRAIN=K12 / MC4100;
RX PubMed=9880556; DOI=10.1074/jbc.274.3.1745;
RA Pellicer M.T., Fernandez C., Badia J., Aguilar J., Lin E.C., Baldom L.;
RT "Cross-induction of glc and ace operons of Escherichia coli attributable to
RT pathway intersection. Characterization of the glc promoter.";
RL J. Biol. Chem. 274:1745-1752(1999).
CC -!- FUNCTION: Component of a complex that catalyzes the oxidation of
CC glycolate to glyoxylate (PubMed:4557653, PubMed:8606183). Is required
CC for E.coli to grow on glycolate as a sole source of carbon
CC (PubMed:8606183). Is also able to oxidize D-lactate ((R)-lactate) with
CC a similar rate (PubMed:4557653). Does not link directly to O(2), and
CC 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act
CC as artificial electron acceptors in vitro, but the physiological
CC molecule that functions as primary electron acceptor during glycolate
CC oxidation is unknown (PubMed:4557653). {ECO:0000269|PubMed:4557653,
CC ECO:0000269|PubMed:8606183}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + glycolate = AH2 + glyoxylate; Xref=Rhea:RHEA:21264,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:29805,
CC ChEBI:CHEBI:36655; EC=1.1.99.14;
CC Evidence={ECO:0000269|PubMed:4557653, ECO:0000305|PubMed:8606183};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21265;
CC Evidence={ECO:0000269|PubMed:8606183, ECO:0000305|PubMed:4557653};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-lactate + A = AH2 + pyruvate; Xref=Rhea:RHEA:15089,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15361, ChEBI:CHEBI:16004,
CC ChEBI:CHEBI:17499; Evidence={ECO:0000269|PubMed:4557653};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- ACTIVITY REGULATION: In vitro the glycolate oxidase activity is
CC inhibited by the sulfhydryl inhibitors CuSO4 and PCMB, by KCN, but not
CC by the metal complexing agent EDTA. {ECO:0000269|PubMed:4557653}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40 uM for glycolate {ECO:0000269|PubMed:4557653};
CC KM=0.7 mM for D-lactate {ECO:0000269|PubMed:4557653};
CC Note=Parameters measured from a partially purified enzyme from
CC extracts of glycolate grown cells. {ECO:0000305|PubMed:4557653};
CC pH dependence:
CC Optimum pH is 8.0-8.8. {ECO:0000269|PubMed:4557653};
CC -!- SUBUNIT: The glycolate oxidase likely consists of three subunits, GlcD,
CC GlcE and GlcF. {ECO:0000269|PubMed:8606183}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:2689218}.
CC Note=Glycolate oxidoreductase activity was shown to be firmly
CC associated with the cytoplasmic membranes.
CC {ECO:0000269|PubMed:2689218}.
CC -!- INDUCTION: Induced in the presence of glycolate or glyoxylate
CC (PubMed:8606183). Part of the glcDEFGB operon, which is induced by
CC growth on glycolate, under the positive control of GlcC. Also induced
CC by growth on acetate. Expression of the glc operon is strongly
CC dependent on the integration host factor (IHF) and is repressed by the
CC global respiratory regulator ArcA-P (PubMed:9880556).
CC {ECO:0000269|PubMed:8606183, ECO:0000269|PubMed:9880556}.
CC -!- DISRUPTION PHENOTYPE: Abolishes glycolate oxidase activity. Is unable
CC to grow on glycolate as the sole source of carbon, in contrast to wild
CC type. {ECO:0000269|PubMed:8606183}.
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000305}.
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DR EMBL; L43490; AAB02530.1; -; Genomic_DNA.
DR EMBL; U28377; AAA69146.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76015.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77040.1; -; Genomic_DNA.
DR PIR; A65084; A65084.
DR RefSeq; NP_417453.1; NC_000913.3.
DR RefSeq; WP_000026117.1; NZ_STEB01000001.1.
DR AlphaFoldDB; P0AEP9; -.
DR BioGRID; 4262368; 16.
DR BioGRID; 851676; 2.
DR IntAct; P0AEP9; 3.
DR STRING; 511145.b2979; -.
DR PaxDb; P0AEP9; -.
DR PRIDE; P0AEP9; -.
DR EnsemblBacteria; AAC76015; AAC76015; b2979.
DR EnsemblBacteria; BAE77040; BAE77040; BAE77040.
DR GeneID; 66673131; -.
DR GeneID; 947353; -.
DR KEGG; ecj:JW2946; -.
DR KEGG; eco:b2979; -.
DR PATRIC; fig|1411691.4.peg.3751; -.
DR EchoBASE; EB2820; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_9_2_6; -.
DR InParanoid; P0AEP9; -.
DR OMA; TPRTCGE; -.
DR PhylomeDB; P0AEP9; -.
DR BioCyc; EcoCyc:G7545-MON; -.
DR BioCyc; MetaCyc:G7545-MON; -.
DR PRO; PR:P0AEP9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009339; C:glycolate oxidase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IEA:InterPro.
DR GO; GO:0047809; F:D-2-hydroxy-acid dehydrogenase activity; IEA:RHEA.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0019154; F:glycolate dehydrogenase activity; IMP:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0046296; P:glycolate catabolic process; IMP:EcoCyc.
DR Gene3D; 1.10.45.10; -; 1.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR004113; FAD-linked_oxidase_C.
DR InterPro; IPR004490; GlcD.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF55103; SSF55103; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR TIGRFAMs; TIGR00387; glcD; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; FAD; Flavoprotein; Membrane;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..499
FT /note="Glycolate oxidase subunit GlcD"
FT /id="PRO_0000128181"
FT DOMAIN 52..230
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ SEQUENCE 499 AA; 53812 MW; 2D850E109DD1BA55 CRC64;
MSILYEERLD GALPDVDRTS VLMALREHVP GLEILHTDEE IIPYECDGLS AYRTRPLLVV
LPKQMEQVTA ILAVCHRLRV PVVTRGAGTG LSGGALPLEK GVLLVMARFK EILDINPVGR
RARVQPGVRN LAISQAVAPH NLYYAPDPSS QIACSIGGNV AENAGGVHCL KYGLTVHNLL
KIEVQTLDGE ALTLGSDALD SPGFDLLALF TGSEGMLGVT TEVTVKLLPK PPVARVLLAS
FDSVEKAGLA VGDIIANGII PGGLEMMDNL SIRAAEDFIH AGYPVDAEAI LLCELDGVES
DVQEDCERVN DILLKAGATD VRLAQDEAER VRFWAGRKNA FPAVGRISPD YYCMDGTIPR
RALPGVLEGI ARLSQQYDLR VANVFHAGDG NMHPLILFDA NEPGEFARAE ELGGKILELC
VEVGGSISGE HGIGREKINQ MCAQFNSDEI TTFHAVKAAF DPDGLLNPGK NIPTLHRCAE
FGAMHVHHGH LPFPELERF
